ORCID Profile
0000-0002-4820-1181
Current Organisations
Wageningen University & Research
,
IT University of Copenhagen
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Publisher: American Chemical Society (ACS)
Date: 05-04-2022
Abstract: Thermal treatment is often employed in food processing to tailor product properties by manipulating the ingredient functionality, but these elevated temperatures may accelerate oxidation and nutrient loss. Here, oxidation of different whey protein systems [α-lactalbumin (α-LA), β-lactoglobulin (β-LG), a mix of α-LA and β-LG (whey model), and a commercial whey protein isolate (WPI)] was investigated during heat treatment at 60-90 °C and a UHT-like treatment by LC-MS-based proteomic analysis. The relative modification levels of each oxidation site were calculated and compared among different heat treatments and s le systems. Oxidation increased significantly in protein systems after heating at ≥90 °C but decreased in systems with higher complexity [pure protein (α-LA > β-LG) > whey model > WPI]. In α-LA, Cys, Met, and Trp residues were found to be most prone to oxidation. In β-LG-containing protein systems, Cys residues were suggested to scavenge most of the reactive oxidants and undergo an oxidation-mediated disulfide rearrangement. The rearranged disulfide bonds contributed to protein aggregation, which was suggested to provide physical protection against oxidation. Overall, limited loss of amino acid residues was detected after acidic hydrolysis followed by UHPLC analysis, which showed only a minor effect of heat treatment on protein oxidation in these protein systems.
Publisher: American Chemical Society (ACS)
Date: 13-01-2022
Abstract: Disulfides are important for maintaining the protein native structure, but they may undergo rearrangement in the presence of free Cys residues, especially under elevated temperatures. Disulfide rearrangement may result in protein aggregation, which is associated with
Publisher: Elsevier BV
Date: 2020
DOI: 10.1016/J.FOODRES.2019.108688
Abstract: Bovine milk shows bacteriostatic activity mainly due to the presence of antibacterial proteins, like lactoferrin, lactoperoxidase and immunoglobulins. Heat treatment is applied to kill bacteria and thereby extend shelf life of dairy products. Such heat treatment may, however, impair the activity of native antibacterial proteins in milk. The aim of this study was to investigate bacteriostatic capacity and retention of antibacterial proteins in unheated and heated bovine milk. Skim milk s les were heated at 65 °C, 70 °C, 75 °C, 80 °C and 85 °C, for 30 min. Whey was isolated from the heat-treated skim milk and the bacteriostatic capacity of this whey was tested against Streptococcus thermophilus, Escherichia coli, Lactococcus lactis and Pseudomonas fluorescens. The proteomic profile of native whey was determined using LC-MS/MS-based proteomics. Results showed that the bacteriostatic activity of whey negatively correlated with intensity of heat treatment, which was also reflected in the reduced level of native antibacterial proteins. There is a significant difference between milk s les treated for 30 min at <75 °C and milk s les treated at ≥75 °C in both bacteriostatic capacity and native antibacterial proteins. Growth rates of Streptococcus thermophilus, Lactococcus lactis and Pseudomonas fluorescens were negatively correlated with retention of lactoferrin and lactoperoxidase. In conclusion, our study shows that the bacteriostatic capacity of whey decreases with increasing heating intensity, which is strongly correlated with the denaturation of antibacterial proteins. Bacteriostatic activity can be a biomarker for loss of function of antibacterial proteins, and can thereby be used as an indicator for the extent of heat processing of dairy products including antibacterial proteins in a mild heat treatment.
Publisher: Elsevier BV
Date: 12-2022
Location: Australia
No related grants have been discovered for Chengkang Li.